Structure formation in short designed peptides probed by proteolytic cleavage.

Abstract:

:The formation of local structure, in short peptides has been probed by examining cleavage patterns and rates of proteolysis of designed sequences with a high tendency to form beta-hairpin structures. Three model sequences which bear fluorescence donor and acceptor groups have been investigated: [see text]. Fluorescence resonance energy transfer (FRET) provides a convenient probe for peptide cleavage. MALDI mass spectrometry has been used to probe sites of cleavage and CD spectroscopy to access the overall backbone conformation using analog sequences, which lack strongly absorbing donor and acceptor groups. The proteases trypsin, subtilisin, collagenase, elastase, proteinase K and thermolysin were used for proteolysis and the rates of cleavage determined. Peptide 3 is the most susceptible to cleavage by all the enzymes except thermolysin, which cleaves all three peptides at comparable rates. Peptides 1 and 2 are completely resistant to the action of trypsin, suggesting that beta-turn formation acts as a deterrent to proteolytic cleavage.

journal_name

Protein Pept Lett

authors

Saikumari YK,Ravindra G,Balaram P

doi

10.2174/092986606776819501

subject

Has Abstract

pub_date

2006-01-01 00:00:00

pages

471-6

issue

5

eissn

0929-8665

issn

1875-5305

journal_volume

13

pub_type

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